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Biochemical studies and crystal structure determination of dihydrodipicolinate synthase from pseudomonas aeruginosa

Analyse Biochemical studies and crystal structure determination of dihydrodipicolinate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PS7
Type: protein
Length: 584 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrodipicolinate synthase
EC: 4.2.1.52
UniProt: D1MH64
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dihydrodipicolinate synthase (EC 4.2.1.52)	protein	292	48% helix, 13% strand	D1MH64

Ligands and binding sites

PGO · S-1,2-propanediol · additive · 7 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	416	0.73	0.83	53	empty
2	131	0.50	0.80	26	empty
3	127	0.50	0.80	25	empty
4	63	0.27	0.73	17	empty

Interfaces

1 interface between chains.

A–B · 1540 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

3PS7 · Biochemical studies and crystal structure determination of dihydrodipicolinate synthase… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt D1MH64
Elsewhere: RCSB PDB 3PS7 · PDBe 3PS7 · UniProt D1MH64

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